RMD5A_MOUSE
ID RMD5A_MOUSE Reviewed; 391 AA.
AC Q80YQ8; E9QNK7; Q3TPH1; Q3UFE2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase RMND5A;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6GLP4};
DE AltName: Full=Protein RMD5 homolog A;
GN Name=Rmnd5a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC complex that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1. MAEA and RMND5A are both required for
CC catalytic activity of the CTLH E3 ubiquitin-protein ligase complex.
CC Catalytic activity of the complex is required for normal cell
CC proliferation. The CTLH E3 ubiquitin-protein ligase complex is not
CC required for the degradation of enzymes involved in gluconeogenesis,
CC such as FBP1. {ECO:0000250|UniProtKB:Q9H871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9H871};
CC -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA,
CC RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and
CC YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q9H871}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9H871}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H871}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE28619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK148556; BAE28619.1; ALT_INIT; mRNA.
DR EMBL; AK164384; BAE37765.1; -; mRNA.
DR EMBL; AC154001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050876; AAH50876.1; -; mRNA.
DR CCDS; CCDS20231.1; -.
DR RefSeq; NP_077250.2; NM_024288.2.
DR RefSeq; XP_006506602.1; XM_006506539.2.
DR AlphaFoldDB; Q80YQ8; -.
DR SMR; Q80YQ8; -.
DR BioGRID; 212873; 3.
DR STRING; 10090.ENSMUSP00000002292; -.
DR iPTMnet; Q80YQ8; -.
DR PhosphoSitePlus; Q80YQ8; -.
DR EPD; Q80YQ8; -.
DR MaxQB; Q80YQ8; -.
DR PaxDb; Q80YQ8; -.
DR PeptideAtlas; Q80YQ8; -.
DR PRIDE; Q80YQ8; -.
DR ProteomicsDB; 300409; -.
DR Antibodypedia; 32147; 211 antibodies from 21 providers.
DR DNASU; 68477; -.
DR Ensembl; ENSMUST00000002292; ENSMUSP00000002292; ENSMUSG00000002222.
DR GeneID; 68477; -.
DR KEGG; mmu:68477; -.
DR UCSC; uc009cgt.2; mouse.
DR CTD; 64795; -.
DR MGI; MGI:1915727; Rmnd5a.
DR VEuPathDB; HostDB:ENSMUSG00000002222; -.
DR eggNOG; KOG2817; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_020227_3_1_1; -.
DR InParanoid; Q80YQ8; -.
DR OMA; QEWLAMK; -.
DR OrthoDB; 987270at2759; -.
DR PhylomeDB; Q80YQ8; -.
DR TreeFam; TF315176; -.
DR BioGRID-ORCS; 68477; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rmnd5a; mouse.
DR PRO; PR:Q80YQ8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80YQ8; protein.
DR Bgee; ENSMUSG00000002222; Expressed in thymus and 259 other tissues.
DR ExpressionAtlas; Q80YQ8; baseline and differential.
DR Genevisible; Q80YQ8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR CDD; cd16794; dRING_RMD5A; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037680; RMD5A_dRING.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_LisH.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..391
FT /note="E3 ubiquitin-protein ligase RMND5A"
FT /id="PRO_0000272649"
FT DOMAIN 114..146
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 153..210
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 336..377
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H871"
FT CONFLICT 80
FT /note="K -> R (in Ref. 1; BAE37765)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="P -> S (in Ref. 3; AAH50876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 43993 MW; A6043EBEED61FBB7 CRC64;
MDQCVTVERE LEKVLHKFSG YGQLCERGLE ELIDYTGGLK HEILQSHGQD AELSGTLSLV
LTQCCKRIKD TVQKLASDHK DIHSSVSRVG KAIDKNFDSD ISSVGIDGCW QADSQRLLNE
VMVEHFFRQG MLDVAEELCQ ESGLSVDPSQ KEPFVELNRI LEALKVRVLR PALEWAVSNR
EMLIAQNSSL EFKLHRLYFI SLLMGGTTNQ REALQYAKNF QPFALNHQKD IQVLMGSLVY
LRQGIENSPY VHLLDANQWA DICDIFTRDA CALLGLSVES PLSVSFSAGC VALPALINIK
AVIEQRQCTG VWNQKDELPI EVDLGKKCWY HSIFACPILR QQTTDNNPPM KLVCGHIISR
DALNKMFNGS KLKCPYCPME QSPGDAKQIF F
